| pubmed-article:2658053 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2658053 | lifeskim:mentions | umls-concept:C1552130 | lld:lifeskim |
| pubmed-article:2658053 | lifeskim:mentions | umls-concept:C1749876 | lld:lifeskim |
| pubmed-article:2658053 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:2658053 | lifeskim:mentions | umls-concept:C1514661 | lld:lifeskim |
| pubmed-article:2658053 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
| pubmed-article:2658053 | pubmed:issue | 4906 | lld:pubmed |
| pubmed-article:2658053 | pubmed:dateCreated | 1989-6-23 | lld:pubmed |
| pubmed-article:2658053 | pubmed:abstractText | Chemical probing methods have been used to "footprint" 16S ribosomal RNA (rRNA) at each step during the in vitro assembly of twenty 30S subunit ribosomal proteins. These experiments yield information about the location of each protein relative to the structure of 16S rRNA and provide the basis for derivation of a detailed model for the three-dimensional folding of 16S rRNA. Several lines of evidence suggest that protein-dependent conformational changes in 16S rRNA play an important part in the cooperativity of ribosome assembly and in fine-tuning of the conformation and dynamics of 16S rRNA in the 30S subunit. | lld:pubmed |
| pubmed-article:2658053 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2658053 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2658053 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2658053 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2658053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2658053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2658053 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2658053 | pubmed:month | May | lld:pubmed |
| pubmed-article:2658053 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:2658053 | pubmed:author | pubmed-author:NollerH FHF | lld:pubmed |
| pubmed-article:2658053 | pubmed:author | pubmed-author:SternSS | lld:pubmed |
| pubmed-article:2658053 | pubmed:author | pubmed-author:ChangchienL... | lld:pubmed |
| pubmed-article:2658053 | pubmed:author | pubmed-author:PowersTT | lld:pubmed |
| pubmed-article:2658053 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2658053 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:2658053 | pubmed:volume | 244 | lld:pubmed |
| pubmed-article:2658053 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2658053 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2658053 | pubmed:pagination | 783-90 | lld:pubmed |
| pubmed-article:2658053 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2658053 | pubmed:meshHeading | pubmed-meshheading:2658053-... | lld:pubmed |
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| pubmed-article:2658053 | pubmed:meshHeading | pubmed-meshheading:2658053-... | lld:pubmed |
| pubmed-article:2658053 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2658053 | pubmed:articleTitle | RNA-protein interactions in 30S ribosomal subunits: folding and function of 16S rRNA. | lld:pubmed |
| pubmed-article:2658053 | pubmed:affiliation | Thimann Laboratories, University of California, Santa Cruz 95064. | lld:pubmed |
| pubmed-article:2658053 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2658053 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2658053 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2658053 | pubmed:publicationType | Review | lld:pubmed |
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